Robert V. Stahelin

Robert V. Stahelin Profile Picture

Retter Professor of Pharmacy
P.h.D. University of Illinois at Chicago

Contact Info:

rstaheli@purdue.edu
TEL: 765-494-4152
DLR 446
https://thestahelinlab.weebly.com/ 

Training Group(s):
Microbiology, Immunology and Infectious Diseases
Membrane Biology
Biomolecular Structure and Biophysics

Active Mentor - currently hosting PULSe students for laboratory rotations and recruiting PULSe students into the laboratory; serves on preliminary exam committees

Current Research Interests:

Interdisciplinary research focused on biological membranes has revealed them as signaling and trafficking platforms for processes fundamental to life. Biomembranes harbor receptors, ion channels, lipid domains, lipid signals, and scaffolding complexes, which function to maintain cellular growth, metabolism, and homeostasis. Moreover, abnormalities in lipid metabolism attributed to genetic changes among other causes are often associated with diseases such as cancer, arthritis and diabetes. Pathogens, including viruses, and bacteria, often hijack human components of lipid metabolism and replicate using biological membranes as platforms or utilize lipids to produce energy during the replication cycle. Thus, there is a need to comprehensively understand molecular events occurring within and on membranes as a means of grasping disease etiology and identifying viable targets for drug development. The main focus of the lab is mechanisms by which lipid-enveloped viruses (coronaviruses, filoviruses and paramyxoviruses) replicate via assembly and budding in human cells to form new virus particles. The lab uses an array of biochemical and biophysical techniques (including structural biology) in vitro and in cells to come to quantitative and confident conclusions in mechanisms by which viral proteins hijack host cell lipids and proteins for their replication cycle.

Selected Publications:

Lipid-specific oligomerization of the Marburg virus matrix protein VP40 is regulated by two distinct interfaces for virion assembly. Amiar S, Husby ML, Wijesinghe KJ, Angel S, Bhattarai N, Gerstman BS, Chapagain PP, Li S, Stahelin RV. J Biol Chem. 2021 May 18:100796.

SARS-CoV-2 viral budding and entry can be modeled using BSL-2 level virus-like particles. Plescia CB, David EA, Patra D, Sengupta R, Amiar S, Su Y, Stahelin RV. J Biol Chem. 2020 Nov 19;296:100103.

The Minor Matrix Protein VP24 from Ebola Virus Lacks Direct Lipid-Binding Properties. Su Y, Stahelin RV. Viruses. 2020 Aug 8;12(8):869.

Mutation of Hydrophobic Residues in the C-Terminal Domain of the Marburg Virus Matrix Protein VP40 Disrupts Trafficking to the Plasma Membrane. Wijesinghe KJ, McVeigh L, Husby ML, Bhattarai N, Ma J, Gerstman BS, Chapagain PP, Stahelin RV. Viruses. 2020 Apr 24;12(4):482.

The Ebola virus matrix protein VP40 hijacks the host plasma membrane to form virus envelope. Amiar S, Stahelin RV. J Lipid Res. 2020 Jul;61(7):971.

A cationic, C-terminal patch and structural rearrangements in Ebola virus matrix VP40 protein control its interactions with phosphatidylserine. Del Vecchio K, Frick CT, Gc JB, Oda SI, Gerstman BS, Saphire EO, Chapagain PP, Stahelin RV. J Biol Chem. 2018 Mar 2;293(9):3335-3349.

Detection of lipid-induced structural changes of the Marburg virus matrix protein VP40 using hydrogen/deuterium exchange-mass spectrometry. Wijesinghe KJ, Urata S, Bhattarai N, Kooijman EE, Gerstman BS, Chapagain PP, Li S, Stahelin RV. J Biol Chem. 2017 Apr 14;292(15):6108-6122.

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